Source:http://linkedlifedata.com/resource/pubmed/id/20483786
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2010-5-20
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pubmed:abstractText |
Viral infection activates transcription factors, such as NF-kappaB and IFN regulatory factor 3, which collaborate to induce type I IFNs and elicit innate antiviral response. Virus-induced signaling adaptor (VISA) has been identified as a critical adaptor required for virus-triggered induction of type I IFNs. In this study, we showed that the E3 ubiquitin ligase RING-finger protein 5 (RNF5) interacted with VISA at mitochondria in a viral infection-dependent manner. Domain mapping experiments indicated that the C-terminal transmembrane domain of VISA was required for its interaction with RNF5. RNF5 targeted VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection, whereas knockdown of RNF5 reversed virus-induced downregulation of VISA at the early phase. These findings suggest that RNF5-mediated ubiquitination and degradation of VISA is one of the mechanisms of the regulation of virus-triggered induction of type I IFNs and cellular antiviral response.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNF5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/VISA protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1550-6606
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
184
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6249-55
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pubmed:meshHeading |
pubmed-meshheading:20483786-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:20483786-Animals,
pubmed-meshheading:20483786-DNA-Binding Proteins,
pubmed-meshheading:20483786-Humans,
pubmed-meshheading:20483786-Immunoblotting,
pubmed-meshheading:20483786-Immunoprecipitation,
pubmed-meshheading:20483786-Mice,
pubmed-meshheading:20483786-Mutagenesis, Site-Directed,
pubmed-meshheading:20483786-Signal Transduction,
pubmed-meshheading:20483786-Transfection,
pubmed-meshheading:20483786-Ubiquitination,
pubmed-meshheading:20483786-Virus Diseases
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pubmed:year |
2010
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pubmed:articleTitle |
The E3 ubiquitin ligase RNF5 targets virus-induced signaling adaptor for ubiquitination and degradation.
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pubmed:affiliation |
College of Life Sciences, Wuhan University, Wuhan, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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